BMRB Entry 25244
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25244
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Title: 1H, 15N and 13C resonance assignments of the RRM1 domain of the key post-transcriptional regulator HuR PubMed: 25487676
Deposition date: 2014-09-23 Original release date: 2015-09-04
Authors: Mujo, Amanda; Lixa, Carolina; Anobom, Cristiane; Almeida, Fabio; Pinheiro, Anderson
Citation: Mujo, Amanda; Lixa, Carolina; Carneiro, Letcia; Anobom, Cristiane; Almeida, Fabio; Pinheiro, Anderson. "1H, 15N and 13C resonance assignments of the RRM1 domain of the key post-transcriptional regulator HuR" Biomol. NMR Assign. 9, 281-284 (2015).
Assembly members:
HuR_RRM1, polymer, 101 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: RP1B
Entity Sequences (FASTA):
HuR_RRM1: GHMSNGYEDHMAEDCRGDIG
RTNLIVNYLPQNMTQDELRS
LFSSIGEVESAKLIRDKVAG
HSLGYGFVNYVTAKDAERAI
NTLNGLRLQSKTIKVSYARP
S
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 412 |
15N chemical shifts | 106 |
1H chemical shifts | 666 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity | 1 |
Entities:
Entity 1, entity 101 residues - Formula weight is not available
Residues Gly-1 and His0 represent a cloning artifact and are derived from the TEV protease clevage site.
1 | GLY | HIS | MET | SER | ASN | GLY | TYR | GLU | ASP | HIS | ||||
2 | MET | ALA | GLU | ASP | CYS | ARG | GLY | ASP | ILE | GLY | ||||
3 | ARG | THR | ASN | LEU | ILE | VAL | ASN | TYR | LEU | PRO | ||||
4 | GLN | ASN | MET | THR | GLN | ASP | GLU | LEU | ARG | SER | ||||
5 | LEU | PHE | SER | SER | ILE | GLY | GLU | VAL | GLU | SER | ||||
6 | ALA | LYS | LEU | ILE | ARG | ASP | LYS | VAL | ALA | GLY | ||||
7 | HIS | SER | LEU | GLY | TYR | GLY | PHE | VAL | ASN | TYR | ||||
8 | VAL | THR | ALA | LYS | ASP | ALA | GLU | ARG | ALA | ILE | ||||
9 | ASN | THR | LEU | ASN | GLY | LEU | ARG | LEU | GLN | SER | ||||
10 | LYS | THR | ILE | LYS | VAL | SER | TYR | ALA | ARG | PRO | ||||
11 | SER |
Samples:
sample_1: HuR_RRM1, [U-100% 15N], 1.5 mM; sodium phosphate 30 mM; sodium chloride 100 mM; DTT 10 mM; H2O 90%; D2O 10%
sample_2: HuR_RRM1, [U-100% 13C; U-100% 15N], 1.5 mM; sodium phosphate 30 mM; sodium chloride 100 mM; DTT 10 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D (H)CC(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HC(C)H-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CARA v1.8.4, Prof. Kurt Wuttrich's group, ETH - chemical shift assignment
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts